High Affinity Electrostatic Interactions Support the Formation of CdS Quantum Dot:Nitrogenase MoFe Protein Complexes

Lauren Pellows, Mark Willis, Jesse Ruzicka, Bhanu Jagilinki, David Mulder, Zhi-Yong Zang, Lance Seefeldt, Paul King, Gordana Dukovic, John Peters

Research output: Contribution to journalArticlepeer-review

Abstract

Nitrogenase MoFe protein can be coupled with CdS nanocrystals (NCs) to enable photocatalytic N2 reduction. The nature of interactions that support complex formation is of paramount importance in intermolecular electron transfer that supports catalysis. In this work we have employed microscale thermophoresis to examine binding interactions between 3-mercaptopropionate capped CdS quantum dots (QDs) and MoFe protein over a range of QD diameters (3.4-4.3 nm). The results indicate that the interactions are largely electrostatic, with the strength of interactions similar to that observed for the physiological electron donor. In addition, the strength of interactions is sensitive to the QD diameter, and the binding interactions are significantly stronger for QDs with smaller diameters. The ability to quantitatively assess NC protein interactions in biohybrid systems supports strategies for understanding properties and reaction parameters that are important for obtaining optimal rates of catalysis in biohybrid systems.
Original languageAmerican English
JournalNano Letters
DOIs
StatePublished - 2023

NREL Publication Number

  • NREL/JA-2700-87515

Keywords

  • electron transfer
  • microscope thermophoresis
  • nitrogen reduction
  • nitrogenase
  • photocatalysis
  • quantum dots

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